1dub: Difference between revisions

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[[Image:1dub.jpg|left|200px]]


<!--
==2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5==
The line below this paragraph, containing "STRUCTURE_1dub", creates the "Structure Box" on the page.
<StructureSection load='1dub' size='340' side='right'caption='[[1dub]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dub]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DUB FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr>
{{STRUCTURE_1dub| PDB=1dub |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dub OCA], [https://pdbe.org/1dub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dub RCSB], [https://www.ebi.ac.uk/pdbsum/1dub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dub ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ECHM_RAT ECHM_RAT] Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/du/1dub_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dub ConSurf].
<div style="clear:both"></div>


'''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5'''
==See Also==
 
*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme catalyses the reversible addition of water to alpha,beta-unsaturated enoyl-CoA thioesters, with nearly diffusion-controlled reaction rates for the best substrates. Enoyl-CoA hydratase is a hexamer of six identical subunits of 161 kDa molecular mass for the complex. The hexamer is a dimer of trimers. The monomer is folded into a right-handed spiral of four turns, followed by two small domains which are involved in trimerization. Each turn of the spiral consists of two beta-strands and an alpha-helix. The mechanism for the hydratase/dehydratase reaction follows a syn-stereochemistry, a preference that is opposite to the nonenzymatic reaction. The active-site architecture agrees with this stereochemistry. It confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction. The comparison of an unliganded and a liganded active site within the same crystal form shows a water molecule in the unliganded subunit. This water molecule is bound between the two catalytic glutamates and could serve as the activated water during catalysis.
[[Category: Large Structures]]
 
==About this Structure==
1DUB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUB OCA].
 
==Reference==
Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket., Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK, EMBO J. 1996 Oct 1;15(19):5135-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8895557 8895557]
[[Category: Enoyl-CoA hydratase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Engel CK]]
[[Category: Engel, C K.]]
[[Category: Wierenga RK]]
[[Category: Wierenga, R K.]]
[[Category: Beta-oxidation]]
[[Category: Coa]]
[[Category: Crotonase]]
[[Category: Enoyl-coa hydratase]]
[[Category: Fatty acid metabolism]]
[[Category: Lyase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:17:01 2008''
Retrieved from "https://proteopedia.org/1dub"